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Database: PDB
Entry: 2JKB
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HEADER    LYASE                                   26-AUG-08   2JKB              
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANB IN                 
TITLE    2 COMPLEX WITH 2,7-ANHYDRO-NEU5AC                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE B;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 30-697;                                           
COMPND   5 SYNONYM: NEURAMINIDASE B, NANB;                                      
COMPND   6 EC: 4.2.2.15;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 170187;                                              
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    INTRAMOLECULAR TRANS-SIALIDASE, LYASE, GLYCOSIDASE,                   
KEYWDS   2 NEURAMINIDASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.GUT,S.J.KING,M.A.WALSH                                              
REVDAT   3   24-FEB-09 2JKB    1       VERSN                                    
REVDAT   2   11-NOV-08 2JKB    1       JRNL   REMARK                            
REVDAT   1   16-SEP-08 2JKB    0                                                
JRNL        AUTH   H.GUT,S.J.KING,M.A.WALSH                                     
JRNL        TITL   STRUCTURAL AND FUNCTIONAL STUDIES OF STREPTOCOCCUS           
JRNL        TITL 2 PNEUMONIAE NEURAMINIDASE B: AN INTRAMOLECULAR                
JRNL        TITL 3 TRANS-SIALIDASE.                                             
JRNL        REF    FEBS LETT.                    V. 582  3348 2008              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   18775704                                                     
JRNL        DOI    10.1016/J.FEBSLET.2008.08.026                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 105364                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2677                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.54                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.58                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6299                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5439                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 1024                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.073         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.047         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.258         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5616 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3785 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7631 ; 1.344 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9281 ; 0.803 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   716 ; 6.919 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   262 ;35.570 ;25.153       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   977 ;11.123 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;13.412 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   826 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6417 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1134 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   967 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4044 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2775 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3063 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   769 ; 0.137 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    15 ; 0.226 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    51 ; 0.315 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    71 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4467 ; 0.984 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5599 ; 1.102 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2591 ; 1.912 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2032 ; 2.555 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2JKB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-AUG-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-37278.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL CUT                 
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONICS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108114                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.54                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.6                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.35                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: HOMOLOGY MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.7                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 200 MM TRIS PH             
REMARK 280  8.0                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.35950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.03950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.37300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.03950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.35950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.37300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     HIS A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     PHE A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     LEU A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2222  -  O    HOH A  2940              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 262   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  51       63.99   -113.65                                   
REMARK 500    ALA A  78       89.52   -153.57                                   
REMARK 500    LYS A  80       57.08   -142.25                                   
REMARK 500    GLN A 240       18.22     59.68                                   
REMARK 500    ILE A 246       61.84     67.06                                   
REMARK 500    SER A 273     -171.45   -171.82                                   
REMARK 500    ASP A 327       88.71     68.56                                   
REMARK 500    PRO A 534       40.89    -86.16                                   
REMARK 500    TYR A 651      119.56   -160.45                                   
REMARK 500    ALA A 652     -120.42   -125.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  365     ASN A  366                  -39.37                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKD A1698                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1699                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VW0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM                        
REMARK 900   STREPTOCOCCUS PNEUMONIAE                                           
REMARK 900 RELATED ID: 2VW1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM                        
REMARK 900   STREPTOCOCCUS PNEUMONIAE                                           
REMARK 900 RELATED ID: 2VW2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM                        
REMARK 900   STREPTOCOCCUS PNEUMONIAE                                           
DBREF  2JKB A   12    29  PDB    2JKB     2JKB            12     29             
DBREF  2JKB A   30   697  UNP    Q54727   NANB_STRPN      30    697             
SEQRES   1 A  686  ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL          
SEQRES   2 A  686  LEU PHE GLN GLY PRO ASN GLU LEU ASN TYR GLY GLN LEU          
SEQRES   3 A  686  SER ILE SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU          
SEQRES   4 A  686  ASN ASN LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP          
SEQRES   5 A  686  LYS LEU SER GLY GLU SER GLN THR VAL VAL MET LYS PHE          
SEQRES   6 A  686  LYS ALA ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY          
SEQRES   7 A  686  LEU SER ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE          
SEQRES   8 A  686  SER ILE PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU          
SEQRES   9 A  686  ILE ARG ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER          
SEQRES  10 A  686  ARG PRO ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA          
SEQRES  11 A  686  VAL GLU ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP          
SEQRES  12 A  686  LYS THR TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE          
SEQRES  13 A  686  SER GLU THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE          
SEQRES  14 A  686  ASN GLY ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG          
SEQRES  15 A  686  GLU GLY LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP          
SEQRES  16 A  686  GLU ILE SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU          
SEQRES  17 A  686  VAL SER THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE          
SEQRES  18 A  686  PHE GLN SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG          
SEQRES  19 A  686  ILE PRO THR LEU TYR THR LEU SER SER GLY ARG VAL LEU          
SEQRES  20 A  686  SER SER ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER          
SEQRES  21 A  686  LYS SER LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP          
SEQRES  22 A  686  ASN GLY LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS          
SEQRES  23 A  686  PHE ASN ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG          
SEQRES  24 A  686  ASP ASN LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA          
SEQRES  25 A  686  SER PHE ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER          
SEQRES  26 A  686  GLY LYS THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY          
SEQRES  27 A  686  ILE GLY ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE          
SEQRES  28 A  686  LYS GLU ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS          
SEQRES  29 A  686  ASN GLY ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN          
SEQRES  30 A  686  GLY VAL VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN          
SEQRES  31 A  686  TYR THR ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY          
SEQRES  32 A  686  LYS SER LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP          
SEQRES  33 A  686  SER GLY SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL          
SEQRES  34 A  686  PRO MET ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL          
SEQRES  35 A  686  THR PRO THR ASN TYR ILE ALA MET THR THR SER GLN ASN          
SEQRES  36 A  686  ARG GLY GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO          
SEQRES  37 A  686  PHE LEU GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO          
SEQRES  38 A  686  GLY GLN GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE          
SEQRES  39 A  686  PHE ALA THR TYR THR SER GLY GLU LEU THR TYR LEU ILE          
SEQRES  40 A  686  SER ASP ASP SER GLY GLN THR TRP LYS LYS SER SER ALA          
SEQRES  41 A  686  SER ILE PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET          
SEQRES  42 A  686  VAL GLU LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG          
SEQRES  43 A  686  THR THR THR GLY LYS ILE ALA TYR MET THR SER ARG ASP          
SEQRES  44 A  686  SER GLY GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY          
SEQRES  45 A  686  ILE GLN GLN THR SER TYR GLY THR GLN VAL SER ALA ILE          
SEQRES  46 A  686  LYS TYR SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE          
SEQRES  47 A  686  LEU SER THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY          
SEQRES  48 A  686  GLN LEU VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER          
SEQRES  49 A  686  ILE ASP TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER          
SEQRES  50 A  686  TYR GLY TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN          
SEQRES  51 A  686  HIS HIS ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP          
SEQRES  52 A  686  SER ARG ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR          
SEQRES  53 A  686  ILE ASP LEU GLU ILE ASN ASP LEU THR LYS                      
HET    SKD  A1698      20                                                       
HET    EDO  A1699       4                                                       
HET    EDO  A1700       4                                                       
HET    EDO  A1701       4                                                       
HET    EDO  A1702       4                                                       
HET    EDO  A1703       4                                                       
HET    EDO  A1704       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SKD 2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-                         
HETNAM   2 SKD  HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-5-                       
HETNAM   3 SKD  CARBOXYLIC ACID                                                 
FORMUL   2  EDO    6(C2 H6 O2)                                                  
FORMUL   3  SKD    C11 H17 N O8                                                 
FORMUL   4  HOH   *1024(H2 O1)                                                  
HELIX    1   1 ILE A   57  LEU A   62  1                                   6    
HELIX    2   2 ASP A   63  LEU A   65  5                                   3    
HELIX    3   3 PRO A  176  ILE A  180  5                                   5    
HELIX    4   4 SER A  216  THR A  222  1                                   7    
HELIX    5   5 GLU A  691  THR A  696  1                                   6    
SHEET    1  AA 6 PHE A  43  ASN A  51  0                                        
SHEET    2  AA 6 LYS A 202  PHE A 211 -1  O  GLY A 203   N  LEU A  50           
SHEET    3  AA 6 GLN A  70  LYS A  77 -1  O  THR A  71   N  PHE A 211           
SHEET    4  AA 6 ASN A 144  ASP A 151 -1  O  ASN A 144   N  PHE A  76           
SHEET    5  AA 6 THR A 156  VAL A 161 -1  O  THR A 156   N  ASP A 151           
SHEET    6  AA 6 ILE A 164  THR A 170 -1  O  ILE A 164   N  VAL A 161           
SHEET    1  AB 6 ILE A  55  ASP A  56  0                                        
SHEET    2  AB 6 LYS A 185  LEU A 188 -1  O  LEU A 188   N  ILE A  55           
SHEET    3  AB 6 LEU A  84  SER A  91 -1  O  GLY A  89   N  THR A 187           
SHEET    4  AB 6 TYR A 101  ARG A 107 -1  O  PHE A 102   N  LEU A  90           
SHEET    5  AB 6 ILE A 112  ASP A 118 -1  O  GLY A 113   N  PHE A 105           
SHEET    6  AB 6 ILE A 123  ARG A 129 -1  O  ILE A 123   N  ASP A 118           
SHEET    1  AC 2 LYS A 136  HIS A 137  0                                        
SHEET    2  AC 2 GLN A 140  ALA A 141 -1  O  GLN A 140   N  HIS A 137           
SHEET    1  AD 2 VAL A 191  ARG A 193  0                                        
SHEET    2  AD 2 LYS A 196  HIS A 198 -1  O  LYS A 196   N  ARG A 193           
SHEET    1  AE 3 TYR A 243  ARG A 245  0                                        
SHEET    2  AE 3 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245           
SHEET    3  AE 3 TYR A 250  THR A 251 -1  O  TYR A 250   N  LEU A 258           
SHEET    1  AF 4 TYR A 243  ARG A 245  0                                        
SHEET    2  AF 4 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245           
SHEET    3  AF 4 ILE A 275  SER A 282 -1  O  ASN A 276   N  ALA A 263           
SHEET    4  AF 4 ILE A 293  MET A 296 -1  O  ILE A 293   N  THR A 279           
SHEET    1  AG 5 LYS A 475  LEU A 476  0                                        
SHEET    2  AG 5 TYR A 458  SER A 464 -1  O  MET A 461   N  LYS A 475           
SHEET    3  AG 5 THR A 339  MET A 346 -1  O  THR A 339   N  SER A 464           
SHEET    4  AG 5 SER A 324  GLU A 332 -1  O  SER A 324   N  MET A 346           
SHEET    5  AG 5 GLY A 493  GLN A 494  1  O  GLY A 493   N  ILE A 330           
SHEET    1  AH 7 PHE A 362  GLU A 364  0                                        
SHEET    2  AH 7 TYR A 369  LYS A 375 -1  O  TYR A 370   N  LYS A 363           
SHEET    3  AH 7 TYR A 383  VAL A 385 -1  O  TYR A 383   N  LEU A 373           
SHEET    4  AH 7 VAL A 390  ASN A 393 -1  O  TYR A 392   N  THR A 384           
SHEET    5  AH 7 LYS A 398  ILE A 404 -1  O  LYS A 398   N  ASN A 393           
SHEET    6  AH 7 VAL A 410  GLU A 412 -1  O  LEU A 411   N  THR A 403           
SHEET    7  AH 7 LYS A 415  SER A 416 -1  O  LYS A 415   N  GLU A 412           
SHEET    1  AI 3 PHE A 362  GLU A 364  0                                        
SHEET    2  AI 3 TYR A 369  LYS A 375 -1  O  TYR A 370   N  LYS A 363           
SHEET    3  AI 3 PHE A 451  LYS A 452 -1  O  LYS A 452   N  LYS A 374           
SHEET    1  AJ 2 THR A 418  ASP A 425  0                                        
SHEET    2  AJ 2 ARG A 432  PRO A 441 -1  O  ARG A 432   N  ASP A 425           
SHEET    1  AK 3 TYR A 489  LEU A 490  0                                        
SHEET    2  AK 3 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489           
SHEET    3  AK 3 LEU A 496  ALA A 497 -1  O  LEU A 496   N  ILE A 505           
SHEET    1  AL 4 TYR A 489  LEU A 490  0                                        
SHEET    2  AL 4 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489           
SHEET    3  AL 4 GLU A 513  SER A 519 -1  O  GLU A 513   N  THR A 510           
SHEET    4  AL 4 LYS A 527  SER A 532 -1  O  LYS A 527   N  ILE A 518           
SHEET    1  AM 4 ALA A 542  ARG A 548  0                                        
SHEET    2  AM 4 VAL A 551  PHE A 556 -1  O  VAL A 551   N  LEU A 547           
SHEET    3  AM 4 ALA A 564  SER A 568 -1  O  ALA A 564   N  PHE A 556           
SHEET    4  AM 4 SER A 579  TYR A 580 -1  O  SER A 579   N  TYR A 565           
SHEET    1  AN 4 SER A 594  ILE A 602  0                                        
SHEET    2  AN 4 LYS A 605  PRO A 613 -1  O  LYS A 605   N  ILE A 602           
SHEET    3  AN 4 GLY A 622  VAL A 629 -1  O  GLN A 623   N  THR A 612           
SHEET    4  AN 4 ILE A 636  ASP A 643 -1  O  ASP A 637   N  LEU A 628           
SHEET    1  AO 3 SER A 654  GLU A 658  0                                        
SHEET    2  AO 3 ILE A 664  GLU A 669 -1  O  GLY A 665   N  THR A 657           
SHEET    3  AO 3 VAL A 685  LEU A 690 -1  O  GLN A 686   N  PHE A 668           
CISPEP   1 SER A  271    LYS A  272          0         2.64                     
SITE     1 AC1 17 ARG A 245  ILE A 246  ARG A 264  ASP A 270                    
SITE     2 AC1 17 ILE A 326  ASP A 327  ASP A 344  ASN A 352                    
SITE     3 AC1 17 THR A 539  GLU A 541  ARG A 557  ARG A 619                    
SITE     4 AC1 17 TYR A 653  TRP A 674  HOH A2457  HOH A3012                    
SITE     5 AC1 17 HOH A3013                                                     
SITE     1 AC2  7 LEU A  84  SER A 103  GLU A 115  TYR A 199                    
SITE     2 AC2  7 LYS A 335  HOH A3014  HOH A3015                               
SITE     1 AC3  6 TYR A 458  ILE A 459  LEU A 477  PRO A 478                    
SITE     2 AC3  6 PHE A 480  HOH A3016                                          
SITE     1 AC4 10 VAL A 385  ILE A 404  ASN A 405  ASP A 406                    
SITE     2 AC4 10 TYR A 408  LYS A 475  HOH A2629  HOH A3017                    
SITE     3 AC4 10 HOH A3018  HOH A3019                                          
SITE     1 AC5  6 THR A 251  GLN A 494  ILE A 596  THR A 657                    
SITE     2 AC5  6 HOH A2956  HOH A3020                                          
SITE     1 AC6  6 SER A 617  LYS A 620  SER A 648  HOH A2911                    
SITE     2 AC6  6 HOH A3021  HOH A3022                                          
SITE     1 AC7  8 ARG A 256  ASN A 466  ARG A 467  GLU A 469                    
SITE     2 AC7  8 SER A 617  HOH A2444  HOH A3023  HOH A3024                    
CRYST1   76.719   82.746  118.079  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013035  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012085  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008469        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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